Role of beta-turn residues in beta-hairpin formation and stability in designed peptides

Ramirez-Alvarado M, Blanco FJ, Niemann H, Serrano L (1997)
J Mol Biol 273(4): 898-912.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Ramirez-Alvarado, M.; Blanco, F. J.; Niemann, HartmutUniBi ; Serrano, L.
Einrichtung
Fakultät für Chemie > Biochemie IV
Stichworte
Amino Acid Sequence; Databases; Circular Dichroism; *Protein Structure; Solutions; *Drug Design; Secondary; Factual; Molecular; Models; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Protein Folding; Protein Engineering/*methods
Erscheinungsjahr
1997
Zeitschriftentitel
J Mol Biol
Band
273
Ausgabe
4
Seite(n)
898-912
ISSN
0022-2836
Page URI
https://pub.uni-bielefeld.de/record/1927957

Zitieren

Ramirez-Alvarado M, Blanco FJ, Niemann H, Serrano L. Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J Mol Biol. 1997;273(4):898-912.
Ramirez-Alvarado, M., Blanco, F. J., Niemann, H., & Serrano, L. (1997). Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J Mol Biol, 273(4), 898-912. https://doi.org/10.1006/jmbi.1997.1347
Ramirez-Alvarado, M., Blanco, F. J., Niemann, Hartmut, and Serrano, L. 1997. “Role of beta-turn residues in beta-hairpin formation and stability in designed peptides”. J Mol Biol 273 (4): 898-912.
Ramirez-Alvarado, M., Blanco, F. J., Niemann, H., and Serrano, L. (1997). Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J Mol Biol 273, 898-912.
Ramirez-Alvarado, M., et al., 1997. Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J Mol Biol, 273(4), p 898-912.
M. Ramirez-Alvarado, et al., “Role of beta-turn residues in beta-hairpin formation and stability in designed peptides”, J Mol Biol, vol. 273, 1997, pp. 898-912.
Ramirez-Alvarado, M., Blanco, F.J., Niemann, H., Serrano, L.: Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J Mol Biol. 273, 898-912 (1997).
Ramirez-Alvarado, M., Blanco, F. J., Niemann, Hartmut, and Serrano, L. “Role of beta-turn residues in beta-hairpin formation and stability in designed peptides”. J Mol Biol 273.4 (1997): 898-912.

73 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Structural characterization of NRAS isoform 5.
Markowitz J, Mal TK, Yuan C, Courtney NB, Patel M, Stiff AR, Blachly J, Walker C, Eisfeld AK, de la Chapelle A, Carson WE., Protein Sci 25(5), 2016
PMID: 26947772
Design of self-assembling peptide hydrogelators amenable to bacterial expression.
Sonmez C, Nagy KJ, Schneider JP., Biomaterials 37(), 2015
PMID: 25453938
AHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides.
Kumar R, Chaudhary K, Sharma M, Nagpal G, Chauhan JS, Singh S, Gautam A, Raghava GP., Nucleic Acids Res 43(database issue), 2015
PMID: 25392419
In silico platform for predicting and initiating β-turns in a protein at desired locations.
Singh H, Singh S, Raghava GP., Proteins 83(5), 2015
PMID: 25728793
PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues.
Singh S, Singh H, Tuknait A, Chaudhary K, Singh B, Kumaran S, Raghava GP., Biol Direct 10(), 2015
PMID: 26690490
Structural and sequence features of two residue turns in beta-hairpins.
Madan B, Seo SY, Lee SG., Proteins 82(9), 2014
PMID: 24488781
Redesigning the type II' β-turn in green fluorescent protein to type I': implications for folding kinetics and stability.
Madan B, Sokalingam S, Raghunathan G, Lee SG., Proteins 82(10), 2014
PMID: 25044033
The interplay of turn formation and hydrophobic interactions on the early kinetic events in protein folding.
Huang JJ, Larsen RW, Chan SI., Chem Commun (Camb) 48(4), 2012
PMID: 22053320
Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: interaction with model membranes.
Sánchez-Martín MJ, Cruz A, Busquets MA, Haro I, Alsina MA, Pujol M., Int J Pharm 436(1-2), 2012
PMID: 22868231
Structure change of β-hairpin induced by turn optimization: an enhanced sampling molecular dynamics simulation study.
Shao Q, Yang L, Gao YQ., J Chem Phys 135(23), 2011
PMID: 22191904
Elimination of a cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding.
Jakob RP, Zierer BK, Weininger U, Hofmann SD, Lorenz SH, Balbach J, Dobbek H, Schmid FX., J Mol Biol 399(2), 2010
PMID: 20394751
Trifluoroethanol reveals helical propensity at analogous positions in cytoplasmic domains of three connexins.
Fort AG, Spray DC., Biopolymers 92(3), 2009
PMID: 19226516
Disulfide bonds versus TrpTrp pairs in irregular beta-hairpins: NMR structure of vammin loop 3-derived peptides as a case study.
Mirassou Y, Santiveri CM, Pérez de Vega MJ, González-Muñiz R, Jiménez MA., Chembiochem 10(5), 2009
PMID: 19294654
The use of post-translationally modified peptides for detection of biomarkers of immune-mediated diseases.
Papini AM., J Pept Sci 15(10), 2009
PMID: 19714713
Context-dependence of the contribution of disulfide bonds to beta-hairpin stability.
Santiveri CM, León E, Rico M, Jiménez MA., Chemistry 14(2), 2008
PMID: 17943702
Thermodynamic analysis of beta-sheet secondary structure by backbone thioester exchange.
Hadley EB, Witek AM, Freire F, Peoples AJ, Gellman SH., Angew Chem Int Ed Engl 46(37), 2007
PMID: 17691093
Structural malleability of plasticins: preorganized conformations in solution and relevance for antimicrobial activity.
Bruston F, Lacombe C, Zimmermann K, Piesse C, Nicolas P, El Amri C., Biopolymers 86(1), 2007
PMID: 17309077
Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility.
El Amri C, Bruston F, Joanne P, Lacombe C, Nicolas P., Eur Biophys J 36(8), 2007
PMID: 17622524
Physical-chemical determinants of turn conformations in globular proteins.
Street TO, Fitzkee NC, Perskie LL, Rose GD., Protein Sci 16(8), 2007
PMID: 17656584
A cross-strand Trp Trp pair stabilizes the hPin1 WW domain at the expense of function.
Jäger M, Dendle M, Fuller AA, Kelly JW., Protein Sci 16(10), 2007
PMID: 17766376
Beta-strand flipping and slipping triggered by turn replacement reveal the opportunistic nature of beta-strand pairing.
Makabe K, Yan S, Tereshko V, Gawlak G, Koide S., J Am Chem Soc 129(47), 2007
PMID: 17985889
Kinetics and thermodynamics of type VIII beta-turn formation: a CD, NMR, and microsecond explicit molecular dynamics study of the GDNP tetrapeptide.
Fuchs PF, Bonvin AM, Bochicchio B, Pepe A, Alix AJ, Tamburro AM., Biophys J 90(8), 2006
PMID: 16443656
Structure-function-folding relationship in a WW domain.
Jäger M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW., Proc Natl Acad Sci U S A 103(28), 2006
PMID: 16807295
Analysis and design of turns in alpha-helical hairpins.
Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF., J Mol Biol 346(5), 2005
PMID: 15713492
An N-glucosylated peptide detecting disease-specific autoantibodies, biomarkers of multiple sclerosis.
Lolli F, Mulinacci B, Carotenuto A, Bonetti B, Sabatino G, Mazzanti B, D'Ursi AM, Novellino E, Pazzagli M, Lovato L, Alcaro MC, Peroni E, Pozo-Carrero MC, Nuti F, Battistini L, Borsellino G, Chelli M, Rovero P, Papini AM., Proc Natl Acad Sci U S A 102(29), 2005
PMID: 16014416
Engineering enhanced protein stability through beta-turn optimization: insights for the design of stable peptide beta-hairpin systems.
Simpson ER, Meldrum JK, Bofill R, Crespo MD, Holmes E, Searle MS., Angew Chem Int Ed Engl 44(31), 2005
PMID: 15999372
Artificial di-iron proteins: solution characterization of four helix bundles containing two distinct types of inter-helical loops.
Maglio O, Nastri F, Calhoun JR, Lahr S, Wade H, Pavone V, DeGrado WF, Lombardi A., J Biol Inorg Chem 10(5), 2005
PMID: 16091937
Beta-hairpin formation in aqueous solution and in the presence of trifluoroethanol: a (1)H and (13)C nuclear magnetic resonance conformational study of designed peptides.
Santiveri CM, Pantoja-Uceda D, Rico M, Jiménez MA., Biopolymers 79(3), 2005
PMID: 16078190
Alpha-alpha linking motifs and interhelical orientations.
Engel DE, DeGrado WF., Proteins 61(2), 2005
PMID: 16104016
Chemical shifts provide fold populations and register of beta hairpins and beta sheets.
Fesinmeyer RM, Hudson FM, Olsen KA, White GW, Euser A, Andersen NH., J Biomol NMR 33(4), 2005
PMID: 16341751
Insights into stabilizing weak interactions in designed peptide beta-hairpins.
Searle MS., Biopolymers 76(2), 2004
PMID: 15054898
Enantioselective ester hydrolysis catalyzed by beta-cyclodextrin conjugated with beta-hairpin peptides.
Tsutsumi H, Ikeda H, Mihara H, Ueno A., Bioorg Med Chem Lett 14(3), 2004
PMID: 14741276
Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial.
Santiveri CM, Santoro J, Rico M, Jiménez MA., Protein Sci 13(4), 2004
PMID: 15044739
Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.
Chen RP, Huang JJ, Chen HL, Jan H, Velusamy M, Lee CT, Fann W, Larsen RW, Chan SI., Proc Natl Acad Sci U S A 101(19), 2004
PMID: 15123838
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins.
Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L., Nat Biotechnol 22(10), 2004
PMID: 15361882
Determining beta-sheet stability by Fourier transform infrared difference spectra.
Wang T, Xu Y, Du D, Gai F., Biopolymers 75(2), 2004
PMID: 15356870
Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings.
Meier S, Güthe S, Kiefhaber T, Grzesiek S., J Mol Biol 344(4), 2004
PMID: 15544812
Combinatorial chemistry of beta-hairpins.
Pastor MT, Pérez-Payá E., Mol Divers 6(2), 2003
PMID: 14761164
Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns.
Rotondi KS, Gierasch LM., Biopolymers 71(6), 2003
PMID: 14991674
Turn stability in beta-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns.
Blandl T, Cochran AG, Skelton NJ., Protein Sci 12(2), 2003
PMID: 12538887
Stability of monomeric Cro variants: Isoenergetic transformation of a type I' to a type II' beta-hairpin by single amino acid replacements.
Mollah AK, Stennis RL, Mossing MC., Protein Sci 12(5), 2003
PMID: 12717034
Immunogenicity of peptide-vaccine candidates predicted by molecular dynamics simulations.
Oomen CJ, Hoogerhout P, Bonvin AM, Kuipers B, Brugghe H, Timmermans H, Haseley SR, van Alphen L, Gros P., J Mol Biol 328(5), 2003
PMID: 12729743
Sequence dependence of beta-hairpin structure: comparison of a salt bridge and an aromatic interaction.
Kiehna SE, Waters ML., Protein Sci 12(12), 2003
PMID: 14627727
Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library.
Skelton NJ, Russell S, de Sauvage F, Cochran AG., J Mol Biol 316(5), 2002
PMID: 11884148
Model peptide studies of sequence regions in the elastomeric biomineralization protein, Lustrin A. I. The C-domain consensus-PG-, -NVNCT-motif.
Zhang B, Wustman BA, Morse D, Evans JS., Biopolymers 63(6), 2002
PMID: 11920437
Analysis of the factors that stabilize a designed two-stranded antiparallel beta-sheet.
Espinosa JF, Syud FA, Gellman SH., Protein Sci 11(6), 2002
PMID: 12021448
Identification of a "glycine-loop"-like coiled structure in the 34 AA Pro,Gly,Met repeat domain of the biomineral-associated protein, PM27.
Wustman BA, Santos R, Zhang B, Evans JS., Biopolymers 65(5), 2002
PMID: 12389216
Interplay between hydrophobic cluster and loop propensity in beta-hairpin formation.
Espinosa JF, Muñoz V, Gellman SH., J Mol Biol 306(3), 2001
PMID: 11178900
Elongation of the BH8 beta-hairpin peptide: Electrostatic interactions in beta-hairpin formation and stability.
Ramírez-Alvarado M, Blanco FJ, Serrano L., Protein Sci 10(7), 2001
PMID: 11420440
Role of loops in the folding and stability of yeast phosphoglycerate kinase.
Collinet B, Garcia P, Minard P, Desmadril M., Eur J Biochem 268(19), 2001
PMID: 11589702
Using flexible loop mimetics to extend phi-value analysis to secondary structure interactions.
Ferguson N, Pires JR, Toepert F, Johnson CM, Pan YP, Volkmer-Engert R, Schneider-Mergener J, Daggett V, Oschkinat H, Fersht A., Proc Natl Acad Sci U S A 98(23), 2001
PMID: 11687614
Templating peptide folding on the surface of a micelle: nucleating the formation of a beta-hairpin.
Searle MS, Jourdan M., Bioorg Med Chem Lett 10(10), 2000
PMID: 10843236
Folding of a beta-hairpin peptide derived from the N-terminus of ubiquitin. Conformational preferences of beta-turn residues dictate non-native beta-strand interactions.
Jourdan M, Griffiths-Jones SR, Searle MS., Eur J Biochem 267(12), 2000
PMID: 10848970
Model peptide studies of sequence repeats derived from the intracrystalline biomineralization protein, SM50. II. Pro,Asn-rich tandem repeats.
Zhang B, Xu G, Evans JS., Biopolymers 54(6), 2000
PMID: 10951331
Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding.
Zerella R, Chen PY, Evans PA, Raine A, Williams DH., Protein Sci 9(11), 2000
PMID: 11152124
Position effect of cross-strand side-chain interactions on beta-hairpin formation.
Santiveri CM, Rico M, Jiménez MA., Protein Sci 9(11), 2000
PMID: 11152125
De novo design and structural characterization of proteins and metalloproteins.
DeGrado WF, Summa CM, Pavone V, Nastri F, Lombardi A., Annu Rev Biochem 68(), 1999
PMID: 10872466
Stability of the residual structure in unfolded BPTI in different conditions of temperature and solvent composition measured by disulphide kinetics and double mutant cycle analysis.
Zdanowski K, Dadlez M., J Mol Biol 287(2), 1999
PMID: 10080904
Model peptide studies of sequence repeats derived from the intracrystalline biomineralization protein, SM50. I. GVGGR and GMGGQ repeats.
Xu G, Evans JS., Biopolymers 49(4), 1999
PMID: 10079769
De novo design of a monomeric three-stranded antiparallel beta-sheet.
de Alba E, Santoro J, Rico M, Jiménez MA., Protein Sci 8(4), 1999
PMID: 10211831
Autonomous folding of a peptide corresponding to the N-terminal beta-hairpin from ubiquitin.
Zerella R, Evans PA, Ionides JM, Packman LC, Trotter BW, Mackay JP, Williams DH., Protein Sci 8(6), 1999
PMID: 10386882
The design of linear peptides that fold as monomeric beta-sheet structures.
Lacroix E, Kortemme T, Lopez de la Paz M, Serrano L., Curr Opin Struct Biol 9(4), 1999
PMID: 10449370
Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.
Griffiths-Jones SR, Maynard AJ, Searle MS., J Mol Biol 292(5), 1999
PMID: 10512702
Molecular dynamics simulations of beta-hairpin folding.
Wang H, Varady J, Ng L, Sung SS., Proteins 37(3), 1999
PMID: 10591094
The turn sequence directs beta-strand alignment in designed beta-hairpins.
de Alba E, Rico M, Jiménez MA., Protein Sci 8(11), 1999
PMID: 10595526
Synthesis, folding, and structure of the beta-turn mimic modified B1 domain of streptococcal protein G.
Odaert B, Jean F, Boutillon C, Buisine E, Melnyk O, Tartar A, Lippens G., Protein Sci 8(12), 1999
PMID: 10631995
Formation and stability of beta-hairpin structures in polypeptides.
Blanco F, Ramírez-Alvarado M, Serrano L., Curr Opin Struct Biol 8(1), 1998
PMID: 9519303
Unusual beta-sheet periodicity in small cyclic peptides.
Gibbs AC, Kondejewski LH, Gronwald W, Nip AM, Hodges RS, Sykes BD, Wishart DS., Nat Struct Biol 5(4), 1998
PMID: 9546219
Side-chain effects on peptidyl-prolyl cis/trans isomerisation.
Reimer U, Scherer G, Drewello M, Kruber S, Schutkowski M, Fischer G., J Mol Biol 279(2), 1998
PMID: 9642049
Obligatory steps in protein folding and the conformational diversity of the transition state.
Martinez JC, Pisabarro MT, Serrano L., Nat Struct Biol 5(8), 1998
PMID: 9699637
Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters.
Lacroix E, Viguera AR, Serrano L., J Mol Biol 284(1), 1998
PMID: 9811549
Determinants of strand register in antiparallel beta-sheets of proteins.
Hutchinson EG, Sessions RB, Thornton JM, Woolfson DN., Protein Sci 7(11), 1998
PMID: 9827995
Minimal model systems for beta sheet secondary structure in proteins.
Gellman SH., Curr Opin Chem Biol 2(6), 1998
PMID: 9914187

60 References

Daten bereitgestellt von Europe PubMed Central.

MLEV-17 based two-dimensional homonuclear magnetism transfer spectroscopy
Bax, J. Magn. Reson. 65(), 1985
Evidence for a short linear peptide that folds into native stable β-hairpin in aqueous solution
Blanco, J. Am. Chem. Soc. 115(), 1993
Structure determination of a tetrassacharide
Bothner-By, J. Am. Chem. Soc. 106(), 1984
Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance.
Bradley EK, Thomason JF, Cohen FE, Kosen PA, Kuntz ID., J. Mol. Biol. 215(4), 1990
PMID: 2231722
The role of turns in the structure of an alpha-helical protein.
Brunet AP, Huang ES, Huffine ME, Loeb JE, Weltman RJ, Hecht MH., Nature 364(6435), 1993
PMID: 8332196
Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare turn mutations that prevent the folding of Rop.
Castagnoli L, Vetriani C, Cesareni G., J. Mol. Biol. 237(4), 1994
PMID: 8151699
Stability of α-helices
Chakrabartty, Advan. Protein Chem. 46(), 1995
Conformation of twisted beta-pleated sheets in proteins.
Chothia C., J. Mol. Biol. 75(2), 1973
PMID: 4728692
Interactions responsible for the pH dependence of the beta-hairpin conformational population formed by a designed linear peptide.
de Alba E, Blanco FJ, Jimenez MA, Rico M, Nieto JL., Eur. J. Biochem. 233(1), 1995
PMID: 7588757
Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution
de, Folding design 1(), 1996
Turn residue sequence determines β-hairpin conformation in designed peptides
de, J. Am. Chem. Soc. 119(), 1997

Flory, 1988
Calculation of protein extinction coefficients from amino acid sequence data.
Gill SC, von Hippel PH., Anal. Biochem. 182(2), 1989
PMID: 2610349
Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.
Guntert P, Braun W, Wuthrich K., J. Mol. Biol. 217(3), 1991
PMID: 1847217
Insights of β-hairpin stabilty in aqueous solution from peptides with enforced type I′ and type II′ β-turns
Haque, J. Am. Chem. Soc. 119(), 1997
Selection of representative protein data sets.
Hobohm U, Scharf M, Schneider R, Sander C., Protein Sci. 1(3), 1992
PMID: 1304348
A revised set of potentials for beta-turn formation in proteins.
Hutchinson EG, Thornton JM., Protein Sci. 3(12), 1994
PMID: 7756980
Transfer of a beta-turn structure to a new protein context.
Hynes TR, Kautz RA, Goodman MA, Gill JF, Fox RO., Nature 339(6219), 1989
PMID: 2716830
Engineering alternative beta-turn types in staphylococcal nuclease.
Hynes TR, Hodel A, Fox RO., Biochemistry 33(17), 1994
PMID: 8172877
Quantitative determination of helical propensities from trifluoroethanol titration curves.
Jasanoff A, Fersht AR., Biochemistry 33(8), 1994
PMID: 8117669
A study of the NH-NMR signals of GGXA tetrapeptides in H2O at low temperature
Jiménez, J. Mol. Struct. 143(), 1986
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.
Kabsch W, Sander C., Biopolymers 22(12), 1983
PMID: 6667333
A simple windowless mixing sequence to suppress cross relaxation in TOCSY experiments
Kadkhodaei, J. Magn. Reson. ser. A 104(), 1993
Contact electron-spin coupling of nuclear magnetic moments
Karplus, J. Phys. Chem. 30(), 1995
Intestinal fatty acid binding protein: a specific residue in one turn appears to stabilize the native structure and be responsible for slow refolding.
Kim K, Ramanathan R, Frieden C., Protein Sci. 6(2), 1997
PMID: 9041638
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules.
Kumar A, Ernst RR, Wuthrich K., Biochem. Biophys. Res. Commun. 95(1), 1980
PMID: 7417242
Charge relay at the peptide bond
Llinás, J. Am. Chem. Soc. 97(), 1975
Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities.
Lopez-Hernandez E, Cronet P, Serrano L, Munoz V., J. Mol. Biol. 266(3), 1997
PMID: 9067614
'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.
Merutka G, Dyson HJ, Wright PE., J. Biomol. NMR 5(1), 1995
PMID: 7881270
Measurement of the beta-sheet-forming propensities of amino acids.
Minor DL Jr, Kim PS., Nature 367(6464), 1994
PMID: 8107853
Context is a major determinant of beta-sheet propensity.
Minor DL Jr, Kim PS., Nature 371(6494), 1994
PMID: 8078589
Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.
Munoz V, Serrano L., Proteins 20(4), 1994
PMID: 7731949
Helix design, prediction and stability.
Munoz V, Serrano L., Curr. Opin. Biotechnol. 6(4), 1995
PMID: 7579647
Analysis of the effect of local interactions on protein stability.
Munoz V, Cronet P, Lopez-Hernandez E, Serrano L., Fold Des 1(3), 1996
PMID: 9079379
Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol.
Nelson JW, Kallenbach NR., Proteins 1(3), 1986
PMID: 3449856
Beta-turn propensities as paradigms for the analysis of structural motifs to engineer protein stability.
Ohage EC, Graml W, Walter MM, Steinbacher S, Steipe B., Protein Sci. 6(1), 1997
PMID: 9007995
Multiple quantum filters for elucidating NMR coupling networks
Piantini, J. Am. Chem. Soc. 104(), 1982
Amino-acid substitutions in a surface turn modulate protein stability.
Predki PF, Agrawal V, Brunger AT, Regan L., Nat. Struct. Biol. 3(1), 1996
PMID: 8548455
De novo design and structural analysis of a model beta-hairpin peptide system.
Ramirez-Alvarado M, Blanco FJ, Serrano L., Nat. Struct. Biol. 3(7), 1996
PMID: 8673604
Turns in peptides and proteins
Rose, Advan. Protein Chem. 37(), 1985
A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin.
Searle MS, Williams DH, Packman LC., Nat. Struct. Biol. 2(11), 1995
PMID: 7583674
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
Serrano L., J. Mol. Biol. 254(2), 1995
PMID: 7490751
Beta-hairpin families in globular proteins.
Sibanda BL, Thornton JM., Nature 316(6024), 1985
PMID: 4010788
Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins.
Sippl MJ., J. Mol. Biol. 213(4), 1990
PMID: 2359125
Knowledge-based potentials for proteins
Sippl, Curr. Opin. Struct. Biol. 2(), 1995
Guidelines for protein design: the energetics of beta sheet side chain interactions.
Smith CK, Regan L., Science 270(5238), 1995
PMID: 7481801
Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations.
Smith LJ, Bolin KA, Schwalbe H, MacArthur MW, Thornton JM, Dobson CM., J. Mol. Biol. 255(3), 1996
PMID: 8568893
A convenient and accurate method for the measurement of the values of spin-spin coupling constants
Stonehouse, J. Magn. Reson. A112(), 1995
Economy in protein design
Struthers, J. Am. Chem. Soc. 118(), 1996
Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures.
Swindells MB, MacArthur MW, Thornton JM., Nat. Struct. Biol. 2(7), 1995
PMID: 7664128
Protein denaturation
Tanford, Advan. Protein Chem. 23(), 1968
Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory.
Villegas V, Viguera AR, Aviles FX, Serrano L., Fold Des 1(1), 1996
PMID: 9079361
Side-chain interactions between sulfur-containing amino acids and phenylalanine in alpha-helices.
Viguera AR, Serrano L., Biochemistry 34(27), 1995
PMID: 7612617
The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics.
Viguera AR, Blanco FJ, Serrano L., J. Mol. Biol. 247(4), 1995
PMID: 7723022
Favourable native-like helical local interactions can accelerate protein folding.
Viguera AR, Villegas V, Aviles FX, Serrano L., Fold Des 2(1), 1997
PMID: 9080196
WHATIF
Vriend, J. Mol. Biol. 8(), 1990
Secondary-structure dependent chemical shifts in proteins.
Williamson MP., Biopolymers 29(10-11), 1990
PMID: 2375792
An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs.
Wouters MA, Curmi PM., Proteins 22(2), 1995
PMID: 7567960

Wüthrich, 1982
In vitro evolution of thermodynamically stable turns.
Zhou HX, Hoess RH, DeGrado WF., Nat. Struct. Biol. 3(5), 1996
PMID: 8612075
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